Reviewed, UniProtKB/Swiss-Prot Q27452 (PRP2_BOMMO)

Names and origin

Protein names	Recommended name:     Phenoloxidase subunit 2     EC=1.14.18.1 Alternative name(s):     Tyrosinase 2     PO 2
Organism	Bombyx mori (Silk moth)
Taxonomic identifier	7091 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Bombycidae › Bombycinae › Bombyx

Protein attributes

Sequence length	693 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Ref.1
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O. Ref.1
Cofactor	Binds 2 copper ions per subunit By similarity. UniProtKB P04253
Subunit structure	Heterodimer. Ref.1
Subcellular location	Secreted.
Tissue specificity	Synthesized by hemocytes and released into the hemolymph plasma. Ref.1
Post-translational modification	The N-terminus is blocked. Ref.3
Sequence similarities	Belongs to the tyrosinase family.
Mass spectrometry	Molecular mass is 81105 Da from positions 52 - 693. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Secreted
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Ref.1 Traceable author statement. Source: UniProtKB melanin biosynthetic process from tyrosine Ref.1 Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Ref.1 Traceable author statement. Source: UniProtKB oxygen transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 51	51	Ref.1		PRO_0000035901
	Chain	52 – 693	642	Phenoloxidase subunit 2 Ref.1		PRO_0000035902
Sites
	Metal binding	213	1	Copper A By similarity UniProtKB P04253
	Metal binding	217	1	Copper A By similarity UniProtKB P04253
	Metal binding	243	1	Copper A By similarity UniProtKB P04253
	Metal binding	366	1	Copper B By similarity UniProtKB P04253
	Metal binding	370	1	Copper B By similarity UniProtKB P04253
	Metal binding	406	1	Copper B By similarity UniProtKB P04253
Amino acid modifications
	Glycosylation	26	1	N-linked (GlcNAc...) Potential
	Glycosylation	64	1	N-linked (GlcNAc...) Potential
	Glycosylation	462	1	N-linked (GlcNAc...) Potential
	Glycosylation	494	1	N-linked (GlcNAc...) Potential
	Glycosylation	680	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	433	1	P → Q AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q27452-1 [UniParc]. Last modified January 1, 1999. Version 2. Checksum: 013114DF4CC1A926	FASTA	693	80,119
	10 20 30 40 50 60 MADVFESLEL LFDRPNEPLI TPKGENNSVF QLTEQFLTED YANNGIELNN RFGDDASEKI 70 80 90 100 110 120 PLKNLSKLPE FKIATQLPKD AEFSLFLPKH QEMANELLGV LMDVPENELQ DLLSTCAFAR 130 140 150 160 170 180 VNLNPQLFNY CYSVALMHRR DTRKVRVKNF AEVFPSKFLD SQVFTQARET AAVIPPDVPR 190 200 210 220 230 240 IPIIIPRDYT ATDLEEEHRL AYWREDIGIN LHHYHWHLVY PFTANDLSIV AKDRRGELFF 250 260 270 280 290 300 YMHQQVIARF NCERLCNSLK RVKKFSNWRE PIPEAYFPKL DSLTSSRGWP PRQSGMQWQD 310 320 330 340 350 360 LNRAAEGLFV TIDEMERWRR NVEEAIATGT VRLPNGQTRP LDIDTLGNML ESSALSPNRE 370 380 390 400 410 420 LYGSIHNNGH SFTAYMHDPE HRYLEQFGVI ADEATTMRDP FFYRWHAYID DVFQKHKESA 430 440 450 460 470 480 YVRPYTRSEL ENPGVQVRSV SVETPGGQPN TLNTFWMLSD VNLSRGLDFS DNGPVYARFT 490 500 510 520 530 540 HLNYRHFSYR INVNNTGSSR RTTVRIFITP KFDERNVPWI FSDQRKMCIE MDRFVTVLNA 550 560 570 580 590 600 GENNIVRQST ESSITIPFEQ TFRDLSAQGN DPRRDELATF NYCGCGWPQH MLVPKGTEAG 610 620 630 640 650 660 MPFQLFVMLS NYDLDRIDQD DGKQLTCVEA SSFCGLKDKK YPDRRAMGFP FDRPSSSATS 670 680 690 LQDFILPNMG LQDITIQLQN VTEPNPRNPP MSV

References

[1]	"Molecular cloning of insect pro-phenol oxidase: a copper-containing protein homologous to arthropod hemocyanin." Kawabata T., Yasuhara Y., Ochiai M., Matsuura S., Ashida M. Proc. Natl. Acad. Sci. U.S.A. 92:7774-7778(1995) [PubMed: 7644494] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Kinshu X Showa. Tissue: Hemocyte.
[2]	Asano T., Ashida M. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Reexamination of properties of phenoloxidase isolated from larval hemolymph of the silkworm Bombyx mori." Yasuhara Y., Koizumi Y., Katagiri C., Ashida M. Arch. Biochem. Biophys. 320:14-23(1995) [PubMed: 7793973] [Abstract] Cited for: MASS SPECTROMETRY. Tissue: Hemocyte.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D49371 mRNA. Translation: BAA08369.1. AB048762 mRNA. Translation: BAB41101.1.
RefSeq	NP_001037534.1.
UniGene	Bmo.1389
3D structure databases
SMR	Q27452. Positions 8-677, 71-678.
ModBase	Search...
Genome annotation databases
GeneID	693073.
Phylogenomic databases
OrthoDB	EOG9NZV14.
PhylomeDB	Q27452.
Enzyme and pathway databases
BRENDA	1.14.18.1. 252.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR013788. Hemocyanin. IPR005203. Hemocyanin_C. IPR000896. Hemocyanin_Cu. IPR005204. Hemocyanin_N. IPR014756. Ig_E-set. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit. G3DSA:2.60.40.1520. hemocyanin_C. 1 hit. G3DSA:1.20.1370.10. hemocyanin_N. 1 hit.
PANTHER	PTHR11511. Hemocyanin. 1 hit.
Pfam	PF03723. Hemocyanin_C. 1 hit. PF00372. Hemocyanin_M. 1 hit. PF03722. Hemocyanin_N. 1 hit. [Graphical view]
PRINTS	PR00187. HAEMOCYANIN.
PROSITE	PS00209. HEMOCYANIN_1. 1 hit. PS00210. HEMOCYANIN_2. 1 hit. PS00497. TYROSINASE_1. False negative. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRP2_BOMMO

Accession

Primary (citable) accession number: Q27452

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	January 1, 1999
Last modified:	January 19, 2010
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)